Zinc in PDB 7l52: Crystal Structure of the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Determined By Serial Crystallography

All present enzymatic activity of Crystal Structure of the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Determined By Serial Crystallography:
3.5.2.6;

The structure of Crystal Structure of the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Determined By Serial Crystallography, PDB code: 7l52 was solved by M.Wilamowski, Y.Kim, D.A.Sherrell, A.Lavens, N.Maltseva, M.Endres, G.Babnigg, A.Joachimiak, Center For Structural Genomics Of Infectiousdiseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.65 / 1.85
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	105.668, 105.668, 99.332, 90, 90, 120
R / Rfree (%)	17.5 / 21.7

The binding sites of Zinc atom in the Crystal Structure of the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Determined By Serial Crystallography (pdb code 7l52). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Determined By Serial Crystallography, PDB code: 7l52:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Determined By Serial Crystallography


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Determined By Serial Crystallography within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:5.4 occ:1.00 NE2 A:HIS105 2.1 3.0 1.0 NE2 A:HIS181 2.1 6.0 1.0 O A:HOH563 2.1 8.2 1.0 ND1 A:HIS107 2.1 3.0 1.0 CD2 A:HIS181 3.0 6.6 1.0 CD2 A:HIS105 3.0 2.9 1.0 CE1 A:HIS105 3.0 3.1 1.0 CE1 A:HIS107 3.1 4.7 1.0 CE1 A:HIS181 3.1 4.4 1.0 O A:HOH466 3.1 14.8 0.6 O A:HOH572 3.1 28.2 1.0 CG A:HIS107 3.2 3.5 1.0 CB A:HIS107 3.5 2.9 1.0 ZN A:ZN302 3.6 4.1 0.9 ND1 A:HIS105 4.1 4.7 1.0 CG A:HIS105 4.1 7.6 1.0 CG A:HIS181 4.2 7.6 1.0 OD1 A:ASP109 4.2 3.3 1.0 ND1 A:HIS181 4.2 7.2 1.0 NE2 A:HIS107 4.2 5.8 1.0 CD2 A:HIS110 4.3 4.3 1.0 O A:HOH553 4.3 39.9 1.0 CD2 A:HIS107 4.3 2.9 1.0 NE2 A:HIS110 4.3 6.3 1.0 O A:HOH452 4.8 25.3 1.0 OD2 A:ASP109 4.9 9.9 1.0 CA A:HIS107 4.9 2.9 1.0 CG A:ASP109 5.0 3.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Determined By Serial Crystallography


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Determined By Serial Crystallography within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:4.1 occ:0.86 O A:HOH563 1.8 8.2 1.0 OD2 A:ASP109 2.0 9.9 1.0 NE2 A:HIS110 2.0 6.3 1.0 NE2 A:HIS246 2.1 7.3 1.0 O A:HOH466 2.6 14.8 0.6 CG A:ASP109 2.8 3.5 1.0 CE1 A:HIS110 3.0 4.1 1.0 OD1 A:ASP109 3.0 3.3 1.0 CD2 A:HIS110 3.0 4.3 1.0 CE1 A:HIS246 3.0 7.8 1.0 CD2 A:HIS246 3.1 8.3 1.0 ZN A:ZN301 3.6 5.4 1.0 ND1 A:HIS110 4.0 5.3 1.0 NE2 A:HIS105 4.1 3.0 1.0 CG A:HIS110 4.1 5.3 1.0 ND1 A:HIS246 4.1 6.8 1.0 CE1 A:HIS105 4.2 3.1 1.0 CB A:ASP109 4.2 3.6 1.0 CG A:HIS246 4.2 6.6 1.0 O A:HOH452 4.3 25.3 1.0 O A:HOH572 4.3 28.2 1.0 O A:HOH553 4.6 39.9 1.0 OG A:SER206 4.8 6.2 0.6 NE2 A:HIS181 4.9 6.0 1.0

M.Wilamowski, Y.Kim, D.A.Sherrell, A.Lavens, N.Maltseva, M.Endres, G.Babnigg, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Crystal Structure of the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia Determined By Serial Crystallography To Be Published.